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BTN1_SCHPO
ID   BTN1_SCHPO              Reviewed;         396 AA.
AC   Q9US09;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 120.
DE   RecName: Full=Protein btn1;
GN   Name=btn1 {ECO:0000312|EMBL:CAB63796.1}; ORFNames=SPAC607.09c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-137; GLU-240 AND
RP   VAL-278.
RX   PubMed=16291725; DOI=10.1242/jcs.02656;
RA   Gachet Y., Codlin S., Hyams J.S., Mole S.E.;
RT   "btn1, the Schizosaccharomyces pombe homologue of the human Batten disease
RT   gene CLN3, regulates vacuole homeostasis.";
RL   J. Cell Sci. 118:5525-5536(2005).
RN   [3]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- FUNCTION: Involved in vacuolar transport and vacuole pH homeostasis.
CC       Also required for cytokinesis. {ECO:0000269|PubMed:16291725}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein. Vacuole membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the battenin family. {ECO:0000255}.
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DR   EMBL; CU329670; CAB63796.1; -; Genomic_DNA.
DR   PIR; T50229; T50229.
DR   RefSeq; NP_593598.1; NM_001019029.2.
DR   AlphaFoldDB; Q9US09; -.
DR   SMR; Q9US09; -.
DR   BioGRID; 280059; 469.
DR   STRING; 4896.SPAC607.09c.1; -.
DR   SwissPalm; Q9US09; -.
DR   PaxDb; Q9US09; -.
DR   EnsemblFungi; SPAC607.09c.1; SPAC607.09c.1:pep; SPAC607.09c.
DR   GeneID; 2543645; -.
DR   KEGG; spo:SPAC607.09c; -.
DR   PomBase; SPAC607.09c; btn1.
DR   VEuPathDB; FungiDB:SPAC607.09c; -.
DR   eggNOG; KOG3880; Eukaryota.
DR   HOGENOM; CLU_029663_1_2_1; -.
DR   InParanoid; Q9US09; -.
DR   OMA; WLCNWQV; -.
DR   PhylomeDB; Q9US09; -.
DR   PRO; PR:Q9US09; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0032153; C:cell division site; IDA:PomBase.
DR   GO; GO:0051286; C:cell tip; IDA:PomBase.
DR   GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IDA:PomBase.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IC:PomBase.
DR   GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR   GO; GO:0022857; F:transmembrane transporter activity; ISM:PomBase.
DR   GO; GO:1903826; P:L-arginine transmembrane transport; ISO:PomBase.
DR   GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
DR   InterPro; IPR003492; Battenin_disease_Cln3.
DR   InterPro; IPR018460; Battenin_disease_Cln3_subgr.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   PANTHER; PTHR10981; PTHR10981; 1.
DR   Pfam; PF02487; CLN3; 1.
DR   PIRSF; PIRSF015974; CLN3_BTN1; 1.
DR   PRINTS; PR01315; BATTENIN.
DR   SUPFAM; SSF103473; SSF103473; 1.
PE   1: Evidence at protein level;
KW   Amino-acid transport; Endoplasmic reticulum; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport; Vacuole.
FT   CHAIN           1..396
FT                   /note="Protein btn1"
FT                   /id="PRO_0000065006"
FT   TRANSMEM        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        76..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        138..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        161..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        234..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        296..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        321..341
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         137
FT                   /note="G->A: Retarded location in the endoplasmic
FT                   reticulum; enlarged vacuoles."
FT                   /evidence="ECO:0000269|PubMed:16291725"
FT   MUTAGEN         240
FT                   /note="E->K: Normal trafficking to vacuolar membrane but
FT                   slower than wild-type; enlarged vacuoles."
FT                   /evidence="ECO:0000269|PubMed:16291725"
FT   MUTAGEN         278
FT                   /note="V->F: Normal trafficking to vacuolar membrane but
FT                   slower than wild-type; enlarged vacuoles."
FT                   /evidence="ECO:0000269|PubMed:16291725"
SQ   SEQUENCE   396 AA;  44014 MW;  3550AA3E46936C2D CRC64;
     MIKLRLTKDA KVGCCFLIFG LLNNLLYVII LSAALDLVGA NVSKGVVLLS NIVPSLACKL
     SASILHVHKF KFAKRIGFCV FMSILGMQWI AWSSSVPSKM LGVSLAAISS SFGEISFLHL
     SSRYHSVSLP CWSSGTGLAG LFGASSYLVM TTWFNFSVRS TLIISSFLPL FLLIMYFFVL
     PESESTSPSI NNNYTPIESI DLRAGHVSFN FVNSLKQTFI FMQPYLLSHM FPQFLVYFSE
     YTINIGVAPT LLFPPEKAGF SSFRDFYPTY QTVYQIGVFL SRSSISFFTV PYLRTLAITQ
     FIILLFTILQ SALYLTSSYH FVLFLIFVEG LIGGTVYVNV YHSLQTTESS QRELAISTVG
     SSDSSGIFLA SLVSLFLEPS LCHFQADRGR DWCALT
 
 
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